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PMID:153904

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Citation

Kanazawa, H, Saito, S and Futai, M (1978) Coupling factor ATPase from Escherichia coli. An uncA mutant (uncA401) with defective alpha subunit. J. Biochem. 84:1513-7

Abstract

Inactive coupling factor ATPase (F1) was prepared from an uncoupled mutant (uncA401) of Escherichia coli. Reconstitution of ATPase activity was observed when alpha subunit from wild-type F1 was added to the dissociated inactive F1 and the mixture was dialyzed against buffer containing ATP and Mg2+. ATPase was also reconstituted when the mixture of alpha subunit (wild type) and crude extract from the mutant was dialyzed against the same buffer. These results indicate that the mutant is defective in alpha subunit, suggesting that the uncA401 locus carries the structural gene for alpha subunit, and that this polypeptide plays an essential role in ATPase activity in F1 molecule.

Links

PubMed

Keywords

Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Macromolecular Substances; Mutation

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:ATPA

part_of

GO:0045261: proton-transporting ATP synthase complex, catalytic core F(1)

ECO:0000315: mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete


See also

References

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